Fibroblast activation protein (FAP; FAP-α; seprase) is a type II 95 kDa post-proline cleaving atypical serine protease, closely related to the dipeptidyl peptidases (DPP) DPP-4, DPP-8, and DPP-9 in the prolyl oligopeptidase gene and enzyme family. FAP is conserved throughout chordate evolution, with homologs in human (hFAP), mouse (mFAP), and Xenopus laevis (89 % and 50 % protein sequence identity to hFAP, respectively). FAP expression correlates with tissue remodeling events (Hamson et al. 2014; Liu et al. 2015; Jiang et al. 2016). FAP is also phylogenetically linked to the prototype prolyl oligopeptidase, which is prolyl endopeptidase (PEP; PREP). FAP has both an endopeptidase activity that is similar to but distinct from that of PEP and a DPP activity that is similar to those of DPP4, DPP8, and DPP9 as well as the unrelated peptidase DPP7 (DPP-II).
FAP was originally...
KeywordsHepatic Stellate Cell Oral Squamous Cell Carcinoma Chimeric Antigen Receptor Dipeptidyl Peptidase Fibroblast Activation Protein
MDG is supported by grants 1105238 and 1113842 from the Australian National Health and Medical Research Council.